2h1s

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<StructureSection load='2h1s' size='340' side='right'caption='[[2h1s]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
<StructureSection load='2h1s' size='340' side='right'caption='[[2h1s]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2h1s]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H1S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H1S FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2h1s]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H1S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H1S FirstGlance]. <br>
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</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.45&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GRHPR, GLXR ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glyoxylate_reductase_(NADP(+)) Glyoxylate reductase (NADP(+))], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.79 1.1.1.79] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2h1s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h1s OCA], [https://pdbe.org/2h1s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h1s RCSB], [https://www.ebi.ac.uk/pdbsum/2h1s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h1s ProSAT], [https://www.topsan.org/Proteins/CESG/2h1s TOPSAN]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2h1s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h1s OCA], [https://pdbe.org/2h1s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h1s RCSB], [https://www.ebi.ac.uk/pdbsum/2h1s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h1s ProSAT], [https://www.topsan.org/Proteins/CESG/2h1s TOPSAN]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
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[[https://www.uniprot.org/uniprot/GRHPR_HUMAN GRHPR_HUMAN]] Defects in GRHPR are the cause of hyperoxaluria primary type 2 (HP2) [MIM:[https://omim.org/entry/260000 260000]]; also known as primary hyperoxaluria type II (PH2). HP2 is a disorder where the main clinical manifestation is calcium oxalate nephrolithiasis though chronic as well as terminal renal insufficiency has been described. It is characterized by an elevated urinary excretion of oxalate and L-glycerate.<ref>PMID:10484776</ref>
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[https://www.uniprot.org/uniprot/GRHPR_HUMAN GRHPR_HUMAN] Defects in GRHPR are the cause of hyperoxaluria primary type 2 (HP2) [MIM:[https://omim.org/entry/260000 260000]; also known as primary hyperoxaluria type II (PH2). HP2 is a disorder where the main clinical manifestation is calcium oxalate nephrolithiasis though chronic as well as terminal renal insufficiency has been described. It is characterized by an elevated urinary excretion of oxalate and L-glycerate.<ref>PMID:10484776</ref>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/GRHPR_HUMAN GRHPR_HUMAN]] Enzyme with hydroxy-pyruvate reductase, glyoxylate reductase and D-glycerate dehydrogenase enzymatic activities. Reduces hydroxypyruvate to D-glycerate, glyoxylate to glycolate oxidizes D-glycerate to hydroxypyruvate.
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[https://www.uniprot.org/uniprot/GRHPR_HUMAN GRHPR_HUMAN] Enzyme with hydroxy-pyruvate reductase, glyoxylate reductase and D-glycerate dehydrogenase enzymatic activities. Reduces hydroxypyruvate to D-glycerate, glyoxylate to glycolate oxidizes D-glycerate to hydroxypyruvate.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Bingman, C A]]
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[[Category: Bingman CA]]
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[[Category: Bitto, E]]
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[[Category: Bitto E]]
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[[Category: Structural genomic]]
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[[Category: Phillips Jr GN]]
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[[Category: Phillips, G N]]
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[[Category: Wesenberg GE]]
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[[Category: Wesenberg, G E]]
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[[Category: Cesg]]
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[[Category: Glyoxylate reductase]]
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[[Category: Hydroxypyruvate reductase]]
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[[Category: Oxidoreductase]]
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[[Category: PSI, Protein structure initiative]]
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[[Category: Q9ubq7]]
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Revision as of 09:50, 30 August 2023

Crystal Structure of a Glyoxylate/Hydroxypyruvate reductase from Homo sapiens

PDB ID 2h1s

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